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Protein

Levodione reductase

Gene

lvr

Organism
Leifsonia aquatica (Corynebacterium aquaticum)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the regio- and stereoselective reversible NAD-dependent reduction of (6R)-2,2,6-trimethyl-1,4-cyclohexanedione (levodione) to (4R,6R)-4-hydroxy-2,2,6-trimethylcyclohexanone (actinol).

Catalytic activityi

(4R,6R)-4-hydroxy-2,2,6-trimethylcyclohexanone + NAD+ = (6R)-2,2,6-trimethyl-1,4-cyclohexanedione + NADH.

Enzyme regulationi

Strongly activated by monovalent cations, such as K+, Na+, and NH4+.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei103 – 1031Role in the determination of stereospecificity
Binding sitei152 – 1521Substrate
Active sitei165 – 1651Proton acceptor

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi17 – 4226NAD1 PublicationAdd
BLAST

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

NAD

Names & Taxonomyi

Protein namesi
Recommended name:
Levodione reductase (EC:1.1.1.-)
Alternative name(s):
(6R)-2,2,6-trimethyl-1,4-cyclohexanedione reductase
Gene namesi
Name:lvr
OrganismiLeifsonia aquatica (Corynebacterium aquaticum)
Taxonomic identifieri144185 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaMicrococcalesMicrobacteriaceaeLeifsonia

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi103 – 1031E → A, D, N or Q: 26-fold increase in Km and a much lower enantiomeric excess of the reaction products. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 267267Levodione reductasePRO_0000054721Add
BLAST

Structurei

Secondary structure

1
267
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi15 – 195Combined sources
Turni20 – 223Combined sources
Helixi24 – 3512Combined sources
Beta strandi39 – 457Combined sources
Helixi47 – 6014Combined sources
Beta strandi66 – 705Combined sources
Helixi76 – 9015Combined sources
Beta strandi94 – 985Combined sources
Helixi109 – 1113Combined sources
Helixi114 – 12411Combined sources
Helixi126 – 14217Combined sources
Beta strandi146 – 1505Combined sources
Helixi153 – 1553Combined sources
Beta strandi160 – 1623Combined sources
Helixi163 – 18321Combined sources
Helixi184 – 1863Combined sources
Beta strandi189 – 1957Combined sources
Helixi201 – 21010Combined sources
Helixi215 – 2239Combined sources
Helixi234 – 24411Combined sources
Helixi247 – 2493Combined sources
Beta strandi256 – 2605Combined sources
Turni261 – 2655Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1IY8X-ray1.60A/B/C/D/E/F/G/H1-267[»]
ProteinModelPortaliQ9LBG2.
SMRiQ9LBG2. Positions 10-267.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9LBG2.

Family & Domainsi

Sequence similaritiesi

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
InterProiIPR016040. NAD(P)-bd_dom.
IPR002347. SDR_fam.
[Graphical view]
PANTHERiPTHR24322. PTHR24322. 2 hits.
PRINTSiPR00081. GDHRDH.
PR00080. SDRFAMILY.
SUPFAMiSSF51735. SSF51735. 1 hit.

Sequencei

Sequence statusi: Complete.

Q9LBG2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTATSSPTTR FTDRVVLITG GGSGLGRATA VRLAAEGAKL SLVDVSSEGL
60 70 80 90 100
EASKAAVLET APDAEVLTTV ADVSDEAQVE AYVTATTERF GRIDGFFNNA
110 120 130 140 150
GIEGKQNPTE SFTAAEFDKV VSINLRGVFL GLEKVLKIMR EQGSGMVVNT
160 170 180 190 200
ASVGGIRGIG NQSGYAAAKH GVVGLTRNSA VEYGRYGIRI NAIAPGAIWT
210 220 230 240 250
PMVENSMKQL DPENPRKAAE EFIQVNPSKR YGEAPEIAAV VAFLLSDDAS
260
YVNATVVPID GGQSAAY
Length:267
Mass (Da):27,920
Last modified:October 1, 2000 - v1
Checksum:i6F05C89383500304
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB042262 Genomic DNA. Translation: BAA95121.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB042262 Genomic DNA. Translation: BAA95121.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1IY8X-ray1.60A/B/C/D/E/F/G/H1-267[»]
ProteinModelPortaliQ9LBG2.
SMRiQ9LBG2. Positions 10-267.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiQ9LBG2.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
InterProiIPR016040. NAD(P)-bd_dom.
IPR002347. SDR_fam.
[Graphical view]
PANTHERiPTHR24322. PTHR24322. 2 hits.
PRINTSiPR00081. GDHRDH.
PR00080. SDRFAMILY.
SUPFAMiSSF51735. SSF51735. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "Cloning, sequence analysis, and expression in Escherichia coli of the gene encoding monovalent cation-activated levodione reductase from Corynebacterium aquaticum M-13."
    Yoshisumi A., Wada M., Takagi H., Shimizu S., Nakamori S.
    Biosci. Biotechnol. Biochem. 65:830-836(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: M-13.
  2. "Purification and characterization of monovalent cation-activated levodione reductase from Corynebacterium aquaticum M-13."
    Wada M., Yoshizumi A., Nakamori S., Shimizu S.
    Appl. Environ. Microbiol. 65:4399-4403(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: PARTIAL PROTEIN SEQUENCE, CHARACTERIZATION.
    Strain: M-13.
  3. "The crystal structure and stereospecificity of levodione reductase from Corynebacterium aquaticum M-13."
    Sogabe S., Yoshizumi A., Fukami T.A., Shiratori Y., Shimizu S., Takagi H., Nakamori S., Wada M.
    J. Biol. Chem. 278:19387-19395(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) IN COMPLEX WITH NAD AND INHIBITOR, MUTAGENESIS OF GLU-103.
    Strain: M-13.

Entry informationi

Entry nameiLVR_LEIAQ
AccessioniPrimary (citable) accession number: Q9LBG2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 25, 2003
Last sequence update: October 1, 2000
Last modified: May 11, 2016
This is version 68 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.